Research workbench
AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q60HH1)
Analyse AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q60HH1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q60HH1
- Type
- protein
- Length
- 563 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3949B53a05e1C9A4dbde69b3a8d2CE2F0823a46a
- Molecule
- Tripeptidyl-peptidase 1
- UniProt
- Q60HH1
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripeptidyl-peptidase 1 | protein | 563 | 27% helix, 23% strand | Q60HH1 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.73 | 0.78 | 87 | empty |
| 2 | 59 | 0.56 | 0.89 | 16 | empty |
| 3 | 98 | 0.36 | 0.74 | 17 | empty |
| 4 | 57 | 0.27 | 0.73 | 13 | empty |
| 5 | 55 | 0.24 | 0.71 | 13 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q60HH1
- Elsewhere: UniProt Q60HH1 · AlphaFold DB Q60HH1
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